HEADER VIRAL PROTEIN 17-FEB-24 8S2E TITLE FAB4251-DS-SOSIP COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: VARIABLE HEAVY CHAIN; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: VARIABLE LIGHT CHAIN; COMPND 7 CHAIN: L; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: ENVELOPE GLYCOPROTEIN GP120; COMPND 11 CHAIN: A, E, C; COMPND 12 ENGINEERED: YES; COMPND 13 OTHER_DETAILS: ENVELOPE GLYCOPROTEIN GP120|HUMAN IMMUNODEFICIENCY COMPND 14 VIRUS 1; COMPND 15 MOL_ID: 4; COMPND 16 MOLECULE: ENVELOPE GLYCOPROTEIN GP41; COMPND 17 CHAIN: B, D, F; COMPND 18 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: HIV WHOLE-GENOME VECTOR AA1305#18; SOURCE 13 ORGANISM_TAXID: 672471; SOURCE 14 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 16 MOL_ID: 4; SOURCE 17 ORGANISM_SCIENTIFIC: HIV WHOLE-GENOME VECTOR AA1305#18; SOURCE 18 ORGANISM_TAXID: 672471; SOURCE 19 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 20 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS HIV, VIRAL PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR P.NORTIER,L.PEREZ JRNL AUTH L.PEREZ,M.FOGLIERINI JRNL TITL RAIN: A MACHINE LEARNING-BASED IDENTIFICATION FOR HIV-1 JRNL TITL 2 BNABS. JRNL REF RES SQ 2024 JRNL REFN ISSN 2693-5015 JRNL PMID 38903123 JRNL DOI 10.21203/RS.3.RS-4023897/V1 REMARK 2 REMARK 2 RESOLUTION. 3.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : REAL REMARK 3 REFINEMENT PROTOCOL : OTHER REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.800 REMARK 3 NUMBER OF PARTICLES : 72497 REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE REMARK 3 CORRECTION REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 8S2E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE. REMARK 100 THE DEPOSITION ID IS D_1292136465. REMARK 245 REMARK 245 EXPERIMENTAL DETAILS REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE REMARK 245 SPECIMEN TYPE : NULL REMARK 245 REMARK 245 ELECTRON MICROSCOPE SAMPLE REMARK 245 SAMPLE TYPE : PARTICLE REMARK 245 PARTICLE TYPE : POINT REMARK 245 NAME OF SAMPLE : ENVELOPE GLYCOPROTEIN HUMAN REMARK 245 IMMUNODEFICIENCY VIRUS 1 WITH REMARK 245 FAB REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 2.00 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 6.00 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 15163 REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : FEI FALCON IV (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 900.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2400.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : OTHER REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 39.89 REMARK 245 ILLUMINATION MODE : OTHER REMARK 245 NOMINAL MAGNIFICATION : 165000 REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 300 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, A, E, B, C, D, F, Z, b, REMARK 350 AND CHAINS: d, e, f, g, h, i, j, k, a, REMARK 350 AND CHAINS: m, M, n, N, o, O, p, P, Q, R, REMARK 350 AND CHAINS: S, T, U, c, V, W, X REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 ALA H 114 REMARK 465 SER H 115 REMARK 465 THR H 116 REMARK 465 LYS H 117 REMARK 465 GLY H 118 REMARK 465 PRO H 119 REMARK 465 SER H 120 REMARK 465 VAL H 121 REMARK 465 PHE H 122 REMARK 465 PRO H 123 REMARK 465 LEU H 124 REMARK 465 ALA H 125 REMARK 465 PRO H 126 REMARK 465 SER H 127 REMARK 465 SER H 128 REMARK 465 LYS H 129 REMARK 465 SER H 130 REMARK 465 THR H 131 REMARK 465 SER H 132 REMARK 465 GLY H 133 REMARK 465 GLY H 134 REMARK 465 THR H 135 REMARK 465 ALA H 136 REMARK 465 ALA H 137 REMARK 465 LEU H 138 REMARK 465 GLY H 139 REMARK 465 CYS H 140 REMARK 465 LEU H 141 REMARK 465 VAL H 142 REMARK 465 LYS H 143 REMARK 465 ASP H 144 REMARK 465 TYR H 145 REMARK 465 PHE H 146 REMARK 465 PRO H 147 REMARK 465 GLU H 148 REMARK 465 PRO H 149 REMARK 465 VAL H 150 REMARK 465 THR H 151 REMARK 465 VAL H 152 REMARK 465 SER H 153 REMARK 465 TRP H 154 REMARK 465 ASN H 155 REMARK 465 SER H 156 REMARK 465 GLY H 157 REMARK 465 ALA H 158 REMARK 465 LEU H 159 REMARK 465 THR H 160 REMARK 465 SER H 161 REMARK 465 GLY H 162 REMARK 465 VAL H 163 REMARK 465 HIS H 164 REMARK 465 THR H 165 REMARK 465 PHE H 166 REMARK 465 PRO H 167 REMARK 465 ALA H 168 REMARK 465 VAL H 169 REMARK 465 LEU H 170 REMARK 465 GLN H 171 REMARK 465 SER H 172 REMARK 465 SER H 173 REMARK 465 GLY H 174 REMARK 465 LEU H 175 REMARK 465 TYR H 176 REMARK 465 SER H 177 REMARK 465 LEU H 178 REMARK 465 SER H 179 REMARK 465 SER H 180 REMARK 465 VAL H 181 REMARK 465 VAL H 182 REMARK 465 THR H 183 REMARK 465 VAL H 184 REMARK 465 PRO H 185 REMARK 465 SER H 186 REMARK 465 SER H 187 REMARK 465 SER H 188 REMARK 465 LEU H 189 REMARK 465 GLY H 190 REMARK 465 THR H 191 REMARK 465 GLN H 192 REMARK 465 THR H 193 REMARK 465 TYR H 194 REMARK 465 ILE H 195 REMARK 465 CYS H 196 REMARK 465 ASN H 197 REMARK 465 VAL H 198 REMARK 465 ASN H 199 REMARK 465 HIS H 200 REMARK 465 LYS H 201 REMARK 465 PRO H 202 REMARK 465 SER H 203 REMARK 465 ASN H 204 REMARK 465 THR H 205 REMARK 465 LYS H 206 REMARK 465 VAL H 207 REMARK 465 ASP H 208 REMARK 465 LYS H 209 REMARK 465 LYS H 210 REMARK 465 VAL H 211 REMARK 465 GLU H 212 REMARK 465 PRO H 213 REMARK 465 LYS H 214 REMARK 465 ARG L 108 REMARK 465 THR L 109 REMARK 465 VAL L 110 REMARK 465 ALA L 111 REMARK 465 ALA L 112 REMARK 465 PRO L 113 REMARK 465 SER L 114 REMARK 465 VAL L 115 REMARK 465 PHE L 116 REMARK 465 ILE L 117 REMARK 465 PHE L 118 REMARK 465 PRO L 119 REMARK 465 PRO L 120 REMARK 465 SER L 121 REMARK 465 ASP L 122 REMARK 465 GLU L 123 REMARK 465 GLN L 124 REMARK 465 LEU L 125 REMARK 465 LYS L 126 REMARK 465 SER L 127 REMARK 465 GLY L 128 REMARK 465 THR L 129 REMARK 465 ALA L 130 REMARK 465 SER L 131 REMARK 465 VAL L 132 REMARK 465 VAL L 133 REMARK 465 CYS L 134 REMARK 465 LEU L 135 REMARK 465 LEU L 136 REMARK 465 ASN L 137 REMARK 465 ASN L 138 REMARK 465 PHE L 139 REMARK 465 TYR L 140 REMARK 465 PRO L 141 REMARK 465 ARG L 142 REMARK 465 GLU L 143 REMARK 465 ALA L 144 REMARK 465 LYS L 145 REMARK 465 VAL L 146 REMARK 465 GLN L 147 REMARK 465 TRP L 148 REMARK 465 LYS L 149 REMARK 465 VAL L 150 REMARK 465 ASP L 151 REMARK 465 ASN L 152 REMARK 465 ALA L 153 REMARK 465 LEU L 154 REMARK 465 GLN L 155 REMARK 465 SER L 156 REMARK 465 GLY L 157 REMARK 465 ASN L 158 REMARK 465 SER L 159 REMARK 465 GLN L 160 REMARK 465 GLU L 161 REMARK 465 SER L 162 REMARK 465 VAL L 163 REMARK 465 THR L 164 REMARK 465 GLU L 165 REMARK 465 GLN L 166 REMARK 465 ASP L 167 REMARK 465 SER L 168 REMARK 465 LYS L 169 REMARK 465 ASP L 170 REMARK 465 SER L 171 REMARK 465 THR L 172 REMARK 465 TYR L 173 REMARK 465 SER L 174 REMARK 465 LEU L 175 REMARK 465 SER L 176 REMARK 465 SER L 177 REMARK 465 THR L 178 REMARK 465 LEU L 179 REMARK 465 THR L 180 REMARK 465 LEU L 181 REMARK 465 SER L 182 REMARK 465 LYS L 183 REMARK 465 ALA L 184 REMARK 465 ASP L 185 REMARK 465 TYR L 186 REMARK 465 GLU L 187 REMARK 465 LYS L 188 REMARK 465 HIS L 189 REMARK 465 LYS L 190 REMARK 465 VAL L 191 REMARK 465 TYR L 192 REMARK 465 ALA L 193 REMARK 465 CYS L 194 REMARK 465 GLU L 195 REMARK 465 VAL L 196 REMARK 465 THR L 197 REMARK 465 HIS L 198 REMARK 465 GLN L 199 REMARK 465 GLY L 200 REMARK 465 LEU L 201 REMARK 465 SER L 202 REMARK 465 SER L 203 REMARK 465 PRO L 204 REMARK 465 VAL L 205 REMARK 465 THR L 206 REMARK 465 LYS L 207 REMARK 465 SER L 208 REMARK 465 PHE L 209 REMARK 465 ASN L 210 REMARK 465 ARG L 211 REMARK 465 GLY L 212 REMARK 465 GLU L 213 REMARK 465 CYS L 214 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 OG1 THR C 37 OG1 THR C 499 2.09 REMARK 500 ND2 ASN E 276 O5 NAG k 1 2.11 REMARK 500 ND2 ASN C 133 O5 NAG C 605 2.14 REMARK 500 OG1 THR E 37 OG1 THR E 499 2.15 REMARK 500 ND2 ASN A 386 O5 NAG Q 1 2.16 REMARK 500 ND2 ASN A 276 O5 NAG P 1 2.17 REMARK 500 ND2 ASN E 133 O5 NAG E 601 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 CYS A 247 CA - CB - SG ANGL. DEV. = 6.6 DEGREES REMARK 500 CYS E 247 CA - CB - SG ANGL. DEV. = 7.0 DEGREES REMARK 500 CYS C 54 CA - CB - SG ANGL. DEV. = 8.9 DEGREES REMARK 500 CYS C 247 CA - CB - SG ANGL. DEV. = 7.0 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 GLU H 31 76.22 -104.80 REMARK 500 ASP H 65 -5.21 75.80 REMARK 500 SER H 76 40.41 39.79 REMARK 500 ASN H 100 -163.33 -77.65 REMARK 500 TRP H 100A -158.69 45.98 REMARK 500 GLU L 25 -169.06 -165.20 REMARK 500 LEU L 33 77.19 15.26 REMARK 500 ALA L 51 -1.14 66.24 REMARK 500 SER L 66 -117.96 52.27 REMARK 500 CYS L 88 79.94 -103.53 REMARK 500 ASN A 88 -0.66 69.52 REMARK 500 PRO A 118 59.52 -90.78 REMARK 500 CYS A 196 37.11 -96.20 REMARK 500 ASN A 197 6.17 -157.69 REMARK 500 SER A 199 136.75 176.49 REMARK 500 GLN A 258 -9.74 73.29 REMARK 500 SER A 365 -72.71 -62.16 REMARK 500 ASN A 386 107.76 -56.38 REMARK 500 THR A 387 51.98 -96.60 REMARK 500 LEU A 390 -62.37 -93.34 REMARK 500 SER A 397 86.84 -66.06 REMARK 500 CYS A 433 -168.80 -100.73 REMARK 500 LEU A 483 35.52 -98.96 REMARK 500 GLU A 492 78.97 -110.17 REMARK 500 ASN E 88 -4.52 73.39 REMARK 500 THR E 163 -168.84 -117.50 REMARK 500 SER E 199 120.84 -173.06 REMARK 500 CYS E 201 -168.05 -108.18 REMARK 500 GLN E 258 -5.65 63.55 REMARK 500 LEU E 259 115.42 -166.11 REMARK 500 ALA E 362 -168.53 -121.99 REMARK 500 LEU E 390 -63.45 -94.13 REMARK 500 GLN E 432 42.49 -176.73 REMARK 500 LEU E 483 36.25 -99.23 REMARK 500 CYS C 74 -135.55 -103.28 REMARK 500 PRO C 76 150.10 -47.74 REMARK 500 ASN C 88 9.41 59.95 REMARK 500 SER C 199 146.12 -174.29 REMARK 500 GLN C 258 -10.41 72.48 REMARK 500 ASN C 276 111.18 -161.58 REMARK 500 PRO C 313 99.76 -68.37 REMARK 500 LEU C 483 30.92 -95.63 REMARK 500 ILE D 622 -56.17 -124.41 REMARK 500 ILE F 622 -56.35 -125.30 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 NAG L 301 REMARK 610 NAG L 302 REMARK 610 NAG Z 1 REMARK 610 NAG e 1 REMARK 610 NAG f 1 REMARK 610 NAG g 1 REMARK 610 NAG p 1 REMARK 610 NAG U 1 REMARK 610 NAG c 1 REMARK 610 NAG X 1 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-19665 RELATED DB: EMDB REMARK 900 FAB4251 COMPLEX WITH BG505 SOSIP DBREF 8S2E H 1 214 PDB 8S2E 8S2E 1 214 DBREF 8S2E L 1 214 PDB 8S2E 8S2E 1 214 DBREF 8S2E A 31 503 PDB 8S2E 8S2E 31 503 DBREF 8S2E E 31 503 PDB 8S2E 8S2E 31 503 DBREF 8S2E B 512 663 PDB 8S2E 8S2E 512 663 DBREF 8S2E C 31 503 PDB 8S2E 8S2E 31 503 DBREF 8S2E D 512 663 PDB 8S2E 8S2E 512 663 DBREF 8S2E F 512 663 PDB 8S2E 8S2E 512 663 SEQRES 1 H 220 GLN VAL HIS VAL MET GLN SER GLY ASP GLN VAL LYS LYS SEQRES 2 H 220 PRO GLY ALA SER VAL GLN VAL SER CYS THR THR SER GLY SEQRES 3 H 220 SER SER PHE ILE GLU ASP SER LEU HIS TRP ILE GLN GLN SEQRES 4 H 220 VAL PRO GLY GLN GLU PRO GLU TRP LEU GLY TRP VAL ASN SEQRES 5 H 220 PRO ARG HIS GLY ALA VAL ASN TYR SER TRP LYS ILE ARG SEQRES 6 H 220 ASP ARG ILE THR MET THR ARG ASP ILE SER LYS SER THR SEQRES 7 H 220 MET TYR VAL GLN MET ARG GLY LEU GLN SER ASP ASP THR SEQRES 8 H 220 ALA MET TYR TYR CYS ALA LYS SER ARG ARG GLY ALA ASN SEQRES 9 H 220 TRP ALA LEU TYR TRP GLY TRP GLY THR ARG ILE THR VAL SEQRES 10 H 220 SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU SEQRES 11 H 220 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA SEQRES 12 H 220 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL SEQRES 13 H 220 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL SEQRES 14 H 220 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SEQRES 15 H 220 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU SEQRES 16 H 220 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SEQRES 17 H 220 SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SEQRES 1 L 203 ASP ILE GLN LEU THR GLN SER PRO SER TYR LEU ALA ALA SEQRES 2 L 203 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG GLU SER SEQRES 3 L 203 ASN ASP LEU ASN TRP TYR LEU GLN ARG PRO GLY LYS PRO SEQRES 4 L 203 PRO LYS LEU LEU ILE SER GLY ALA SER LYS LEU GLU ARG SEQRES 5 L 203 GLY VAL PRO SER ARG PHE ARG GLY SER SER SER GLY SER SEQRES 6 L 203 LEU THR ILE SER GLY LEU GLN PRO GLU ASP ILE GLY THR SEQRES 7 L 203 TYR TYR CYS GLN VAL PHE GLU PHE PHE GLY GLY GLY THR SEQRES 8 L 203 ARG VAL ASP ILE LYS ARG THR VAL ALA ALA PRO SER VAL SEQRES 9 L 203 PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY SEQRES 10 L 203 THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO SEQRES 11 L 203 ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU SEQRES 12 L 203 GLN SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SEQRES 13 L 203 SER LYS ASP SER THR TYR SER LEU SER SER THR LEU THR SEQRES 14 L 203 LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA SEQRES 15 L 203 CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR SEQRES 16 L 203 LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 A 441 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 A 441 VAL TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 A 441 ASP HIS ASN VAL TRP ALA THR HIS ALA CYS VAL PRO THR SEQRES 4 A 441 ASP PRO ASN PRO GLN GLU ILE HIS LEU GLU ASN VAL THR SEQRES 5 A 441 GLU GLU PHE ASN MET TRP LYS ASN ASN MET VAL GLU GLN SEQRES 6 A 441 MET HIS THR ASP ILE ILE SER LEU TRP ASP GLN SER LEU SEQRES 7 A 441 LYS PRO CYS VAL LYS LEU THR PRO LEU CYS VAL THR LEU SEQRES 8 A 441 GLN CYS THR ASN VAL THR ASN ASN ILE THR ASP ASP MET SEQRES 9 A 441 ARG GLY GLU LEU LYS ASN CYS SER PHE ASN MET THR THR SEQRES 10 A 441 GLU LEU ARG ASP LYS LYS GLN LYS VAL TYR SER LEU PHE SEQRES 11 A 441 TYR ARG LEU ASP VAL VAL GLN ILE LYS GLU TYR ARG LEU SEQRES 12 A 441 ILE ASN CYS ASN THR SER ALA CYS THR GLN ALA CYS PRO SEQRES 13 A 441 LYS VAL SER PHE GLU PRO ILE PRO ILE HIS TYR CYS ALA SEQRES 14 A 441 PRO ALA GLY PHE ALA ILE LEU LYS CYS LYS ASP LYS LYS SEQRES 15 A 441 PHE ASN GLY THR GLY PRO CYS PRO SER VAL SER THR VAL SEQRES 16 A 441 GLN CYS THR HIS GLY ILE LYS PRO VAL VAL SER THR GLN SEQRES 17 A 441 LEU LEU LEU ASN GLY SER LEU ALA GLU GLU GLU VAL MET SEQRES 18 A 441 ILE ARG SER GLU ASN ILE THR ASN ASN ALA LYS ASN ILE SEQRES 19 A 441 LEU VAL GLN PHE ASN THR PRO VAL GLN ILE ASN CYS THR SEQRES 20 A 441 ARG PRO ASN ASN ASN THR ARG LYS SER ILE ARG ILE GLY SEQRES 21 A 441 PRO GLY GLN ALA PHE TYR ALA THR GLY ASP ILE ILE GLY SEQRES 22 A 441 ASP ILE ARG GLN ALA HIS CYS ASN VAL SER LYS ALA THR SEQRES 23 A 441 TRP ASN GLU THR LEU GLY LYS VAL VAL LYS GLN LEU ARG SEQRES 24 A 441 LYS HIS PHE GLY ASN ASN THR ILE ILE ARG PHE ALA ASN SEQRES 25 A 441 SER SER GLY GLY ASP LEU GLU VAL THR THR HIS SER PHE SEQRES 26 A 441 ASN CYS GLY GLY GLU PHE PHE TYR CYS ASN THR SER GLY SEQRES 27 A 441 LEU PHE ASN SER THR TRP ILE SER ASN SER ASN ASP SER SEQRES 28 A 441 ILE THR LEU PRO CYS ARG ILE LYS GLN ILE ILE ASN MET SEQRES 29 A 441 TRP GLN ARG ILE GLY GLN CYS MET TYR ALA PRO PRO ILE SEQRES 30 A 441 GLN GLY VAL ILE ARG CYS VAL SER ASN ILE THR GLY LEU SEQRES 31 A 441 ILE LEU THR ARG ASP GLY GLY SER THR ASN SER THR THR SEQRES 32 A 441 GLU THR PHE ARG PRO GLY GLY GLY ASP MET ARG ASP ASN SEQRES 33 A 441 TRP ARG SER GLU LEU TYR LYS TYR LYS VAL VAL LYS ILE SEQRES 34 A 441 GLU PRO LEU GLY VAL ALA PRO THR ARG CYS LYS ARG SEQRES 1 E 441 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 E 441 VAL TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 E 441 ASP HIS ASN VAL TRP ALA THR HIS ALA CYS VAL PRO THR SEQRES 4 E 441 ASP PRO ASN PRO GLN GLU ILE HIS LEU GLU ASN VAL THR SEQRES 5 E 441 GLU GLU PHE ASN MET TRP LYS ASN ASN MET VAL GLU GLN SEQRES 6 E 441 MET HIS THR ASP ILE ILE SER LEU TRP ASP GLN SER LEU SEQRES 7 E 441 LYS PRO CYS VAL LYS LEU THR PRO LEU CYS VAL THR LEU SEQRES 8 E 441 GLN CYS THR ASN VAL THR ASN ASN ILE THR ASP ASP MET SEQRES 9 E 441 ARG GLY GLU LEU LYS ASN CYS SER PHE ASN MET THR THR SEQRES 10 E 441 GLU LEU ARG ASP LYS LYS GLN LYS VAL TYR SER LEU PHE SEQRES 11 E 441 TYR ARG LEU ASP VAL VAL GLN ILE LYS GLU TYR ARG LEU SEQRES 12 E 441 ILE ASN CYS ASN THR SER ALA CYS THR GLN ALA CYS PRO SEQRES 13 E 441 LYS VAL SER PHE GLU PRO ILE PRO ILE HIS TYR CYS ALA SEQRES 14 E 441 PRO ALA GLY PHE ALA ILE LEU LYS CYS LYS ASP LYS LYS SEQRES 15 E 441 PHE ASN GLY THR GLY PRO CYS PRO SER VAL SER THR VAL SEQRES 16 E 441 GLN CYS THR HIS GLY ILE LYS PRO VAL VAL SER THR GLN SEQRES 17 E 441 LEU LEU LEU ASN GLY SER LEU ALA GLU GLU GLU VAL MET SEQRES 18 E 441 ILE ARG SER GLU ASN ILE THR ASN ASN ALA LYS ASN ILE SEQRES 19 E 441 LEU VAL GLN PHE ASN THR PRO VAL GLN ILE ASN CYS THR SEQRES 20 E 441 ARG PRO ASN ASN ASN THR ARG LYS SER ILE ARG ILE GLY SEQRES 21 E 441 PRO GLY GLN ALA PHE TYR ALA THR GLY ASP ILE ILE GLY SEQRES 22 E 441 ASP ILE ARG GLN ALA HIS CYS ASN VAL SER LYS ALA THR SEQRES 23 E 441 TRP ASN GLU THR LEU GLY LYS VAL VAL LYS GLN LEU ARG SEQRES 24 E 441 LYS HIS PHE GLY ASN ASN THR ILE ILE ARG PHE ALA ASN SEQRES 25 E 441 SER SER GLY GLY ASP LEU GLU VAL THR THR HIS SER PHE SEQRES 26 E 441 ASN CYS GLY GLY GLU PHE PHE TYR CYS ASN THR SER GLY SEQRES 27 E 441 LEU PHE ASN SER THR TRP ILE SER ASN SER ASN ASP SER SEQRES 28 E 441 ILE THR LEU PRO CYS ARG ILE LYS GLN ILE ILE ASN MET SEQRES 29 E 441 TRP GLN ARG ILE GLY GLN CYS MET TYR ALA PRO PRO ILE SEQRES 30 E 441 GLN GLY VAL ILE ARG CYS VAL SER ASN ILE THR GLY LEU SEQRES 31 E 441 ILE LEU THR ARG ASP GLY GLY SER THR ASN SER THR THR SEQRES 32 E 441 GLU THR PHE ARG PRO GLY GLY GLY ASP MET ARG ASP ASN SEQRES 33 E 441 TRP ARG SER GLU LEU TYR LYS TYR LYS VAL VAL LYS ILE SEQRES 34 E 441 GLU PRO LEU GLY VAL ALA PRO THR ARG CYS LYS ARG SEQRES 1 B 130 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 B 130 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 B 130 THR VAL GLN ALA ARG ASN LEU LEU SER THR VAL TRP GLY SEQRES 4 B 130 ILE LYS GLN LEU GLN ALA ARG VAL LEU ALA VAL GLU ARG SEQRES 5 B 130 TYR LEU ARG ASP GLN GLN LEU LEU GLY ILE TRP GLY CYS SEQRES 6 B 130 SER GLY LYS LEU ILE CYS CYS THR ASN VAL PRO TRP ASN SEQRES 7 B 130 SER SER TRP SER ASN ARG ASN LEU SER GLU ILE TRP ASP SEQRES 8 B 130 ASN MET THR TRP LEU GLN TRP ASP LYS GLU ILE SER ASN SEQRES 9 B 130 TYR THR GLN ILE ILE TYR GLY LEU LEU GLU GLU SER GLN SEQRES 10 B 130 ASN GLN GLN GLU LYS ASN GLU GLN ASP LEU LEU ALA LEU SEQRES 1 C 441 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 C 441 VAL TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 C 441 ASP HIS ASN VAL TRP ALA THR HIS ALA CYS VAL PRO THR SEQRES 4 C 441 ASP PRO ASN PRO GLN GLU ILE HIS LEU GLU ASN VAL THR SEQRES 5 C 441 GLU GLU PHE ASN MET TRP LYS ASN ASN MET VAL GLU GLN SEQRES 6 C 441 MET HIS THR ASP ILE ILE SER LEU TRP ASP GLN SER LEU SEQRES 7 C 441 LYS PRO CYS VAL LYS LEU THR PRO LEU CYS VAL THR LEU SEQRES 8 C 441 GLN CYS THR ASN VAL THR ASN ASN ILE THR ASP ASP MET SEQRES 9 C 441 ARG GLY GLU LEU LYS ASN CYS SER PHE ASN MET THR THR SEQRES 10 C 441 GLU LEU ARG ASP LYS LYS GLN LYS VAL TYR SER LEU PHE SEQRES 11 C 441 TYR ARG LEU ASP VAL VAL GLN ILE LYS GLU TYR ARG LEU SEQRES 12 C 441 ILE ASN CYS ASN THR SER ALA CYS THR GLN ALA CYS PRO SEQRES 13 C 441 LYS VAL SER PHE GLU PRO ILE PRO ILE HIS TYR CYS ALA SEQRES 14 C 441 PRO ALA GLY PHE ALA ILE LEU LYS CYS LYS ASP LYS LYS SEQRES 15 C 441 PHE ASN GLY THR GLY PRO CYS PRO SER VAL SER THR VAL SEQRES 16 C 441 GLN CYS THR HIS GLY ILE LYS PRO VAL VAL SER THR GLN SEQRES 17 C 441 LEU LEU LEU ASN GLY SER LEU ALA GLU GLU GLU VAL MET SEQRES 18 C 441 ILE ARG SER GLU ASN ILE THR ASN ASN ALA LYS ASN ILE SEQRES 19 C 441 LEU VAL GLN PHE ASN THR PRO VAL GLN ILE ASN CYS THR SEQRES 20 C 441 ARG PRO ASN ASN ASN THR ARG LYS SER ILE ARG ILE GLY SEQRES 21 C 441 PRO GLY GLN ALA PHE TYR ALA THR GLY ASP ILE ILE GLY SEQRES 22 C 441 ASP ILE ARG GLN ALA HIS CYS ASN VAL SER LYS ALA THR SEQRES 23 C 441 TRP ASN GLU THR LEU GLY LYS VAL VAL LYS GLN LEU ARG SEQRES 24 C 441 LYS HIS PHE GLY ASN ASN THR ILE ILE ARG PHE ALA ASN SEQRES 25 C 441 SER SER GLY GLY ASP LEU GLU VAL THR THR HIS SER PHE SEQRES 26 C 441 ASN CYS GLY GLY GLU PHE PHE TYR CYS ASN THR SER GLY SEQRES 27 C 441 LEU PHE ASN SER THR TRP ILE SER ASN SER ASN ASP SER SEQRES 28 C 441 ILE THR LEU PRO CYS ARG ILE LYS GLN ILE ILE ASN MET SEQRES 29 C 441 TRP GLN ARG ILE GLY GLN CYS MET TYR ALA PRO PRO ILE SEQRES 30 C 441 GLN GLY VAL ILE ARG CYS VAL SER ASN ILE THR GLY LEU SEQRES 31 C 441 ILE LEU THR ARG ASP GLY GLY SER THR ASN SER THR THR SEQRES 32 C 441 GLU THR PHE ARG PRO GLY GLY GLY ASP MET ARG ASP ASN SEQRES 33 C 441 TRP ARG SER GLU LEU TYR LYS TYR LYS VAL VAL LYS ILE SEQRES 34 C 441 GLU PRO LEU GLY VAL ALA PRO THR ARG CYS LYS ARG SEQRES 1 D 130 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 D 130 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 D 130 THR VAL GLN ALA ARG ASN LEU LEU SER THR VAL TRP GLY SEQRES 4 D 130 ILE LYS GLN LEU GLN ALA ARG VAL LEU ALA VAL GLU ARG SEQRES 5 D 130 TYR LEU ARG ASP GLN GLN LEU LEU GLY ILE TRP GLY CYS SEQRES 6 D 130 SER GLY LYS LEU ILE CYS CYS THR ASN VAL PRO TRP ASN SEQRES 7 D 130 SER SER TRP SER ASN ARG ASN LEU SER GLU ILE TRP ASP SEQRES 8 D 130 ASN MET THR TRP LEU GLN TRP ASP LYS GLU ILE SER ASN SEQRES 9 D 130 TYR THR GLN ILE ILE TYR GLY LEU LEU GLU GLU SER GLN SEQRES 10 D 130 ASN GLN GLN GLU LYS ASN GLU GLN ASP LEU LEU ALA LEU SEQRES 1 F 130 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 F 130 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 F 130 THR VAL GLN ALA ARG ASN LEU LEU SER THR VAL TRP GLY SEQRES 4 F 130 ILE LYS GLN LEU GLN ALA ARG VAL LEU ALA VAL GLU ARG SEQRES 5 F 130 TYR LEU ARG ASP GLN GLN LEU LEU GLY ILE TRP GLY CYS SEQRES 6 F 130 SER GLY LYS LEU ILE CYS CYS THR ASN VAL PRO TRP ASN SEQRES 7 F 130 SER SER TRP SER ASN ARG ASN LEU SER GLU ILE TRP ASP SEQRES 8 F 130 ASN MET THR TRP LEU GLN TRP ASP LYS GLU ILE SER ASN SEQRES 9 F 130 TYR THR GLN ILE ILE TYR GLY LEU LEU GLU GLU SER GLN SEQRES 10 F 130 ASN GLN GLN GLU LYS ASN GLU GLN ASP LEU LEU ALA LEU HET NAG L 301 14 HET NAG L 302 14 HET NAG A 601 14 HET NAG A 602 14 HET NAG A 603 14 HET NAG A 604 14 HET NAG A 605 14 HET NAG E 601 14 HET NAG E 602 14 HET NAG E 603 14 HET NAG E 604 14 HET NAG E 605 14 HET NAG C 601 14 HET NAG C 602 14 HET NAG C 603 14 HET NAG C 604 14 HET NAG C 605 14 HET NAG Z 1 14 HET NAG Z 2 14 HET NAG b 1 14 HET NAG b 2 14 HET BMA b 3 11 HET MAN b 4 11 HET MAN b 5 11 HET NAG d 1 14 HET NAG d 2 14 HET NAG e 1 14 HET NAG e 2 14 HET NAG f 1 14 HET NAG f 2 14 HET NAG g 1 14 HET NAG g 2 14 HET NAG h 1 14 HET NAG h 2 14 HET NAG i 1 14 HET NAG i 2 14 HET NAG j 1 14 HET NAG j 2 14 HET BMA j 3 11 HET NAG k 1 14 HET NAG k 2 14 HET NAG a 1 14 HET NAG a 2 14 HET NAG m 1 14 HET NAG m 2 14 HET BMA m 3 11 HET MAN m 4 11 HET MAN m 5 11 HET NAG M 1 14 HET NAG M 2 14 HET NAG n 1 14 HET NAG n 2 14 HET NAG N 1 14 HET NAG N 2 14 HET NAG o 1 14 HET NAG o 2 14 HET NAG O 1 14 HET NAG O 2 14 HET BMA O 3 11 HET NAG p 1 14 HET NAG p 2 14 HET NAG P 1 14 HET NAG P 2 14 HET NAG Q 1 14 HET NAG Q 2 14 HET NAG R 1 14 HET NAG R 2 14 HET BMA R 3 11 HET MAN R 4 11 HET MAN R 5 11 HET NAG S 1 14 HET NAG S 2 14 HET NAG T 1 14 HET NAG T 2 14 HET NAG U 1 14 HET NAG U 2 14 HET NAG c 1 14 HET NAG c 2 14 HET NAG V 1 14 HET NAG V 2 14 HET NAG W 1 14 HET NAG W 2 14 HET NAG X 1 14 HET NAG X 2 14 HET BMA X 3 11 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM BMA BETA-D-MANNOSE HETNAM MAN ALPHA-D-MANNOSE FORMUL 9 NAG 73(C8 H15 N O6) FORMUL 27 BMA 6(C6 H12 O6) FORMUL 27 MAN 6(C6 H12 O6) HELIX 1 AA1 ARG H 96 ALA H 99 5 4 HELIX 2 AA2 GLN L 79 ILE L 83 5 5 HELIX 3 AA3 ASN A 98 LYS A 117 1 20 HELIX 4 AA4 LEU A 122 CYS A 126 5 5 HELIX 5 AA5 THR A 139 ARG A 151 5 5 HELIX 6 AA6 LYS A 335 GLY A 354 1 20 HELIX 7 AA7 ASP A 368 THR A 373 1 6 HELIX 8 AA8 ASP A 474 SER A 481 1 8 HELIX 9 AA9 ASN E 98 LYS E 117 1 20 HELIX 10 AB1 THR E 139 ARG E 151 5 5 HELIX 11 AB2 LYS E 335 GLY E 354 1 20 HELIX 12 AB3 ASP E 368 THR E 373 1 6 HELIX 13 AB4 MET E 475 SER E 481 1 7 HELIX 14 AB5 LEU B 523 GLY B 527 5 5 HELIX 15 AB6 THR B 529 SER B 534 1 6 HELIX 16 AB7 THR B 536 ARG B 542 1 7 HELIX 17 AB8 VAL B 570 ILE B 595 1 26 HELIX 18 AB9 THR B 627 SER B 636 1 10 HELIX 19 AC1 THR B 639 LEU B 663 1 25 HELIX 20 AC2 ASN C 98 LYS C 117 1 20 HELIX 21 AC3 LEU C 122 CYS C 126 5 5 HELIX 22 AC4 THR C 139 ARG C 151 5 5 HELIX 23 AC5 LYS C 335 GLY C 354 1 20 HELIX 24 AC6 ASP C 368 THR C 373 1 6 HELIX 25 AC7 ASP C 474 SER C 481 1 8 HELIX 26 AC8 LEU D 523 GLY D 527 5 5 HELIX 27 AC9 THR D 529 SER D 534 1 6 HELIX 28 AD1 THR D 536 ASN D 543 1 8 HELIX 29 AD2 VAL D 570 ILE D 595 1 26 HELIX 30 AD3 ASN D 618 ILE D 622 5 5 HELIX 31 AD4 THR D 627 SER D 636 1 10 HELIX 32 AD5 THR D 639 LEU D 663 1 25 HELIX 33 AD6 LEU F 523 GLY F 527 5 5 HELIX 34 AD7 THR F 529 SER F 534 1 6 HELIX 35 AD8 THR F 536 ASN F 543 1 8 HELIX 36 AD9 VAL F 570 ILE F 595 1 26 HELIX 37 AE1 THR F 627 SER F 636 1 10 HELIX 38 AE2 THR F 639 LEU F 663 1 25 SHEET 1 AA1 4 HIS H 3 GLN H 6 0 SHEET 2 AA1 4 VAL H 18 SER H 25 -1 O SER H 25 N HIS H 3 SHEET 3 AA1 4 THR H 77 MET H 82 -1 O MET H 82 N VAL H 18 SHEET 4 AA1 4 THR H 68 ASP H 72 -1 N THR H 68 O GLN H 81 SHEET 1 AA2 6 GLN H 10 VAL H 11 0 SHEET 2 AA2 6 THR H 107 THR H 110 1 O THR H 110 N GLN H 10 SHEET 3 AA2 6 ALA H 88 LYS H 94 -1 N TYR H 90 O THR H 107 SHEET 4 AA2 6 LEU H 34 GLN H 39 -1 N HIS H 35 O ALA H 93 SHEET 5 AA2 6 GLU H 46 VAL H 51 -1 O GLY H 49 N TRP H 36 SHEET 6 AA2 6 VAL H 57 TYR H 59 -1 O ASN H 58 N TRP H 50 SHEET 1 AA3 2 THR L 5 GLN L 6 0 SHEET 2 AA3 2 CYS L 23 ARG L 24 -1 O ARG L 24 N THR L 5 SHEET 1 AA4 3 VAL L 19 THR L 20 0 SHEET 2 AA4 3 LEU L 73 ILE L 75 -1 O ILE L 75 N VAL L 19 SHEET 3 AA4 3 ARG L 63 GLY L 64 -1 N ARG L 63 O THR L 74 SHEET 1 AA5 3 LYS L 45 ILE L 48 0 SHEET 2 AA5 3 ASN L 34 GLN L 38 -1 N LEU L 37 O LYS L 45 SHEET 3 AA5 3 THR L 85 GLN L 89 -1 O THR L 85 N GLN L 38 SHEET 1 AA6 3 GLY A 495 THR A 499 0 SHEET 2 AA6 3 TRP A 35 TYR A 39 -1 N TYR A 39 O GLY A 495 SHEET 3 AA6 3 ILE B 603 PRO B 609 -1 O CYS B 604 N VAL A 38 SHEET 1 AA7 5 TRP A 45 ASP A 47 0 SHEET 2 AA7 5 TYR A 486 ILE A 491 -1 O LYS A 490 N LYS A 46 SHEET 3 AA7 5 PHE A 223 CYS A 228 -1 N ALA A 224 O VAL A 489 SHEET 4 AA7 5 VAL A 242 VAL A 245 -1 O SER A 243 N LYS A 227 SHEET 5 AA7 5 GLU A 83 LEU A 86 -1 N ILE A 84 O THR A 244 SHEET 1 AA8 2 GLU A 91 ASN A 94 0 SHEET 2 AA8 2 THR A 236 CYS A 239 -1 O CYS A 239 N GLU A 91 SHEET 1 AA9 5 LYS A 169 TYR A 177 0 SHEET 2 AA9 5 LEU A 154 THR A 162 -1 N CYS A 157 O SER A 174 SHEET 3 AA9 5 LEU A 129 ASN A 133 -1 N GLN A 130 O SER A 158 SHEET 4 AA9 5 GLU A 190 LEU A 193 -1 O TYR A 191 N LEU A 129 SHEET 5 AA9 5 VAL A 181 GLN A 183 -1 N VAL A 182 O ARG A 192 SHEET 1 AB1 4 LEU A 260 LEU A 261 0 SHEET 2 AB1 4 GLY A 441 LEU A 454 -1 O THR A 450 N LEU A 260 SHEET 3 AB1 4 ILE A 284 ASN A 302 -1 N PHE A 288 O THR A 450 SHEET 4 AB1 4 MET A 271 ARG A 273 -1 N MET A 271 O GLN A 287 SHEET 1 AB2 7 LEU A 260 LEU A 261 0 SHEET 2 AB2 7 GLY A 441 LEU A 454 -1 O THR A 450 N LEU A 260 SHEET 3 AB2 7 ILE A 284 ASN A 302 -1 N PHE A 288 O THR A 450 SHEET 4 AB2 7 HIS A 330 SER A 334 -1 O HIS A 330 N THR A 297 SHEET 5 AB2 7 SER A 413 LYS A 421 -1 O LEU A 416 N CYS A 331 SHEET 6 AB2 7 GLU A 381 CYS A 385 -1 N TYR A 384 O ARG A 419 SHEET 7 AB2 7 HIS A 374 CYS A 378 -1 N CYS A 378 O GLU A 381 SHEET 1 AB3 2 ARG A 304 GLY A 312 0 SHEET 2 AB3 2 GLN A 315 THR A 320 -1 O PHE A 317 N ILE A 307 SHEET 1 AB4 3 SER A 393 ILE A 396 0 SHEET 2 AB4 3 ILE A 358 PHE A 361 -1 N ILE A 359 O TRP A 395 SHEET 3 AB4 3 THR A 465 PHE A 468 1 O PHE A 468 N ARG A 360 SHEET 1 AB5 2 ILE A 423 ILE A 424 0 SHEET 2 AB5 2 MET A 434 TYR A 435 -1 O MET A 434 N ILE A 424 SHEET 1 AB6 3 GLY E 495 THR E 499 0 SHEET 2 AB6 3 TRP E 35 TYR E 39 -1 N TRP E 35 O THR E 499 SHEET 3 AB6 3 ILE F 603 PRO F 609 -1 O CYS F 604 N VAL E 38 SHEET 1 AB7 5 TRP E 45 ASP E 47 0 SHEET 2 AB7 5 TYR E 486 ILE E 491 -1 O LYS E 490 N LYS E 46 SHEET 3 AB7 5 PHE E 223 CYS E 228 -1 N ALA E 224 O VAL E 489 SHEET 4 AB7 5 VAL E 242 VAL E 245 -1 O SER E 243 N LYS E 227 SHEET 5 AB7 5 GLU E 83 LEU E 86 -1 N ILE E 84 O THR E 244 SHEET 1 AB8 3 VAL E 75 PRO E 76 0 SHEET 2 AB8 3 PHE E 53 SER E 56 1 N CYS E 54 O VAL E 75 SHEET 3 AB8 3 HIS E 216 CYS E 218 -1 O CYS E 218 N PHE E 53 SHEET 1 AB9 2 GLU E 91 ASN E 94 0 SHEET 2 AB9 2 THR E 236 CYS E 239 -1 O CYS E 239 N GLU E 91 SHEET 1 AC1 5 LYS E 169 TYR E 177 0 SHEET 2 AC1 5 LEU E 154 THR E 162 -1 N LYS E 155 O PHE E 176 SHEET 3 AC1 5 LEU E 129 ASN E 133 -1 N GLN E 130 O SER E 158 SHEET 4 AC1 5 GLU E 190 LEU E 193 -1 O TYR E 191 N LEU E 129 SHEET 5 AC1 5 VAL E 181 GLN E 183 -1 N VAL E 182 O ARG E 192 SHEET 1 AC2 2 THR E 202 GLN E 203 0 SHEET 2 AC2 2 MET E 434 TYR E 435 1 O TYR E 435 N THR E 202 SHEET 1 AC3 7 LEU E 260 LEU E 261 0 SHEET 2 AC3 7 ILE E 443 ARG E 456 -1 O THR E 450 N LEU E 260 SHEET 3 AC3 7 ILE E 284 ARG E 298 -1 N PHE E 288 O THR E 450 SHEET 4 AC3 7 HIS E 330 SER E 334 -1 O HIS E 330 N THR E 297 SHEET 5 AC3 7 SER E 413 LYS E 421 -1 O ILE E 414 N VAL E 333 SHEET 6 AC3 7 GLU E 381 CYS E 385 -1 N TYR E 384 O ARG E 419 SHEET 7 AC3 7 HIS E 374 CYS E 378 -1 N HIS E 374 O CYS E 385 SHEET 1 AC4 6 MET E 271 ARG E 273 0 SHEET 2 AC4 6 ILE E 284 ARG E 298 -1 O LEU E 285 N ARG E 273 SHEET 3 AC4 6 ILE E 443 ARG E 456 -1 O THR E 450 N PHE E 288 SHEET 4 AC4 6 THR E 465 PRO E 470 -1 O ARG E 469 N THR E 455 SHEET 5 AC4 6 ILE E 358 PHE E 361 1 N ARG E 360 O GLU E 466 SHEET 6 AC4 6 SER E 393 TRP E 395 -1 O TRP E 395 N ILE E 359 SHEET 1 AC5 2 ARG E 304 GLY E 312 0 SHEET 2 AC5 2 GLN E 315 THR E 320 -1 O ALA E 319 N LYS E 305 SHEET 1 AC6 3 GLY C 495 THR C 499 0 SHEET 2 AC6 3 TRP C 35 TYR C 39 -1 N TRP C 35 O THR C 499 SHEET 3 AC6 3 ILE D 603 PRO D 609 -1 O CYS D 604 N VAL C 38 SHEET 1 AC7 5 TRP C 45 ASP C 47 0 SHEET 2 AC7 5 TYR C 486 ILE C 491 -1 O LYS C 490 N LYS C 46 SHEET 3 AC7 5 PHE C 223 CYS C 228 -1 N ALA C 224 O VAL C 489 SHEET 4 AC7 5 VAL C 242 VAL C 245 -1 O SER C 243 N LYS C 227 SHEET 5 AC7 5 GLU C 83 LEU C 86 -1 N ILE C 84 O THR C 244 SHEET 1 AC8 2 GLU C 91 ASN C 94 0 SHEET 2 AC8 2 THR C 236 CYS C 239 -1 O GLY C 237 N PHE C 93 SHEET 1 AC9 5 LYS C 169 TYR C 177 0 SHEET 2 AC9 5 LEU C 154 THR C 162 -1 N CYS C 157 O SER C 174 SHEET 3 AC9 5 LEU C 129 ASN C 133 -1 N GLN C 130 O SER C 158 SHEET 4 AC9 5 GLU C 190 LEU C 193 -1 O TYR C 191 N LEU C 129 SHEET 5 AC9 5 VAL C 181 GLN C 183 -1 N VAL C 182 O ARG C 192 SHEET 1 AD1 3 THR C 202 GLN C 203 0 SHEET 2 AD1 3 MET C 434 TYR C 435 1 O TYR C 435 N THR C 202 SHEET 3 AD1 3 ILE C 423 ILE C 424 -1 N ILE C 424 O MET C 434 SHEET 1 AD2 7 LEU C 260 LEU C 261 0 SHEET 2 AD2 7 ILE C 443 ASP C 457 -1 O THR C 450 N LEU C 260 SHEET 3 AD2 7 ILE C 284 ARG C 298 -1 N ILE C 294 O SER C 447 SHEET 4 AD2 7 HIS C 330 SER C 334 -1 O HIS C 330 N THR C 297 SHEET 5 AD2 7 SER C 413 LYS C 421 -1 O LEU C 416 N CYS C 331 SHEET 6 AD2 7 GLU C 381 CYS C 385 -1 N TYR C 384 O ARG C 419 SHEET 7 AD2 7 HIS C 374 CYS C 378 -1 N HIS C 374 O CYS C 385 SHEET 1 AD3 6 MET C 271 ARG C 273 0 SHEET 2 AD3 6 ILE C 284 ARG C 298 -1 O GLN C 287 N MET C 271 SHEET 3 AD3 6 ILE C 443 ASP C 457 -1 O SER C 447 N ILE C 294 SHEET 4 AD3 6 THR C 465 PRO C 470 -1 O ARG C 469 N THR C 455 SHEET 5 AD3 6 ILE C 358 PHE C 361 1 N ARG C 360 O GLU C 466 SHEET 6 AD3 6 SER C 393 TRP C 395 -1 O SER C 393 N PHE C 361 SHEET 1 AD4 2 ARG C 304 GLY C 312 0 SHEET 2 AD4 2 GLN C 315 THR C 320 -1 O PHE C 317 N ILE C 307 SSBOND 1 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 2 CYS L 23 CYS L 88 1555 1555 2.05 SSBOND 3 CYS A 54 CYS A 74 1555 1555 2.03 SSBOND 4 CYS A 119 CYS A 205 1555 1555 2.04 SSBOND 5 CYS A 126 CYS A 196 1555 1555 2.02 SSBOND 6 CYS A 131 CYS A 157 1555 1555 2.03 SSBOND 7 CYS A 201 CYS A 433 1555 1555 2.03 SSBOND 8 CYS A 218 CYS A 247 1555 1555 2.04 SSBOND 9 CYS A 228 CYS A 239 1555 1555 2.03 SSBOND 10 CYS A 296 CYS A 331 1555 1555 2.03 SSBOND 11 CYS A 378 CYS A 445 1555 1555 2.03 SSBOND 12 CYS A 385 CYS A 418 1555 1555 2.03 SSBOND 13 CYS A 501 CYS B 605 1555 1555 2.03 SSBOND 14 CYS E 54 CYS E 74 1555 1555 2.03 SSBOND 15 CYS E 119 CYS E 205 1555 1555 2.03 SSBOND 16 CYS E 126 CYS E 196 1555 1555 2.03 SSBOND 17 CYS E 131 CYS E 157 1555 1555 2.03 SSBOND 18 CYS E 201 CYS E 433 1555 1555 2.04 SSBOND 19 CYS E 218 CYS E 247 1555 1555 2.04 SSBOND 20 CYS E 228 CYS E 239 1555 1555 2.03 SSBOND 21 CYS E 296 CYS E 331 1555 1555 2.03 SSBOND 22 CYS E 378 CYS E 445 1555 1555 2.03 SSBOND 23 CYS E 385 CYS E 418 1555 1555 2.03 SSBOND 24 CYS E 501 CYS F 605 1555 1555 2.03 SSBOND 25 CYS B 598 CYS B 604 1555 1555 2.03 SSBOND 26 CYS C 54 CYS C 74 1555 1555 2.05 SSBOND 27 CYS C 119 CYS C 205 1555 1555 2.03 SSBOND 28 CYS C 126 CYS C 196 1555 1555 2.02 SSBOND 29 CYS C 131 CYS C 157 1555 1555 2.03 SSBOND 30 CYS C 201 CYS C 433 1555 1555 2.03 SSBOND 31 CYS C 218 CYS C 247 1555 1555 2.04 SSBOND 32 CYS C 228 CYS C 239 1555 1555 2.03 SSBOND 33 CYS C 296 CYS C 331 1555 1555 2.03 SSBOND 34 CYS C 378 CYS C 445 1555 1555 2.03 SSBOND 35 CYS C 385 CYS C 418 1555 1555 2.03 SSBOND 36 CYS C 501 CYS D 605 1555 1555 2.03 SSBOND 37 CYS D 598 CYS D 604 1555 1555 2.03 SSBOND 38 CYS F 598 CYS F 604 1555 1555 2.03 LINK ND2 ASN A 88 C1 NAG O 1 1555 1555 1.45 LINK ND2 ASN A 133 C1 NAG A 605 1555 1555 1.45 LINK ND2 ASN A 156 C1 NAG S 1 1555 1555 1.44 LINK ND2 ASN A 160 C1 NAG N 1 1555 1555 1.44 LINK ND2 ASN A 197 C1 NAG A 604 1555 1555 1.43 LINK ND2 ASN A 234 C1 NAG A 601 1555 1555 1.44 LINK ND2 ASN A 262 C1 NAG R 1 1555 1555 1.44 LINK ND2 ASN A 276 C1 NAG P 1 1555 1555 1.44 LINK ND2 ASN A 295 C1 NAG a 1 1555 1555 1.44 LINK ND2 ASN A 301 C1 NAG A 603 1555 1555 1.46 LINK ND2 ASN A 332 C1 NAG T 1 1555 1555 1.44 LINK ND2 ASN A 386 C1 NAG Q 1 1555 1555 1.44 LINK ND2 ASN A 392 C1 NAG A 602 1555 1555 1.43 LINK ND2 ASN A 448 C1 NAG M 1 1555 1555 1.44 LINK ND2 ASN E 88 C1 NAG j 1 1555 1555 1.46 LINK ND2 ASN E 133 C1 NAG E 601 1555 1555 1.43 LINK ND2 ASN E 156 C1 NAG n 1 1555 1555 1.45 LINK ND2 ASN E 160 C1 NAG i 1 1555 1555 1.44 LINK ND2 ASN E 197 C1 NAG E 605 1555 1555 1.44 LINK ND2 ASN E 234 C1 NAG E 602 1555 1555 1.45 LINK ND2 ASN E 262 C1 NAG m 1 1555 1555 1.43 LINK ND2 ASN E 276 C1 NAG k 1 1555 1555 1.43 LINK ND2 ASN E 301 C1 NAG E 604 1555 1555 1.44 LINK ND2 ASN E 332 C1 NAG o 1 1555 1555 1.45 LINK ND2 ASN E 392 C1 NAG E 603 1555 1555 1.44 LINK ND2 ASN E 448 C1 NAG h 1 1555 1555 1.48 LINK ND2 ASN C 133 C1 NAG C 605 1555 1555 1.43 LINK ND2 ASN C 156 C1 NAG d 1 1555 1555 1.44 LINK ND2 ASN C 160 C1 NAG W 1 1555 1555 1.45 LINK ND2 ASN C 197 C1 NAG C 604 1555 1555 1.43 LINK ND2 ASN C 234 C1 NAG C 601 1555 1555 1.44 LINK ND2 ASN C 262 C1 NAG b 1 1555 1555 1.45 LINK ND2 ASN C 301 C1 NAG C 603 1555 1555 1.45 LINK ND2 ASN C 392 C1 NAG C 602 1555 1555 1.45 LINK ND2 ASN C 448 C1 NAG V 1 1555 1555 1.44 LINK O4 NAG Z 1 C1 NAG Z 2 1555 1555 1.45 LINK O4 NAG b 1 C1 NAG b 2 1555 1555 1.45 LINK O4 NAG b 2 C1 BMA b 3 1555 1555 1.44 LINK O3 BMA b 3 C1 MAN b 4 1555 1555 1.44 LINK O2 MAN b 4 C1 MAN b 5 1555 1555 1.44 LINK O4 NAG d 1 C1 NAG d 2 1555 1555 1.44 LINK O4 NAG e 1 C1 NAG e 2 1555 1555 1.44 LINK O4 NAG f 1 C1 NAG f 2 1555 1555 1.43 LINK O4 NAG g 1 C1 NAG g 2 1555 1555 1.44 LINK O4 NAG h 1 C1 NAG h 2 1555 1555 1.44 LINK O4 NAG i 1 C1 NAG i 2 1555 1555 1.45 LINK O4 NAG j 1 C1 NAG j 2 1555 1555 1.44 LINK O4 NAG j 2 C1 BMA j 3 1555 1555 1.45 LINK O4 NAG k 1 C1 NAG k 2 1555 1555 1.45 LINK O4 NAG a 1 C1 NAG a 2 1555 1555 1.45 LINK O4 NAG m 1 C1 NAG m 2 1555 1555 1.45 LINK O4 NAG m 2 C1 BMA m 3 1555 1555 1.44 LINK O3 BMA m 3 C1 MAN m 4 1555 1555 1.45 LINK O2 MAN m 4 C1 MAN m 5 1555 1555 1.44 LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.45 LINK O4 NAG n 1 C1 NAG n 2 1555 1555 1.44 LINK O4 NAG N 1 C1 NAG N 2 1555 1555 1.44 LINK O4 NAG o 1 C1 NAG o 2 1555 1555 1.44 LINK O4 NAG O 1 C1 NAG O 2 1555 1555 1.44 LINK O4 NAG O 2 C1 BMA O 3 1555 1555 1.44 LINK O4 NAG p 1 C1 NAG p 2 1555 1555 1.45 LINK O4 NAG P 1 C1 NAG P 2 1555 1555 1.45 LINK O4 NAG Q 1 C1 NAG Q 2 1555 1555 1.44 LINK O4 NAG R 1 C1 NAG R 2 1555 1555 1.45 LINK O4 NAG R 2 C1 BMA R 3 1555 1555 1.44 LINK O3 BMA R 3 C1 MAN R 4 1555 1555 1.44 LINK O2 MAN R 4 C1 MAN R 5 1555 1555 1.44 LINK O4 NAG S 1 C1 NAG S 2 1555 1555 1.44 LINK O4 NAG T 1 C1 NAG T 2 1555 1555 1.44 LINK O4 NAG U 1 C1 NAG U 2 1555 1555 1.44 LINK O4 NAG c 1 C1 NAG c 2 1555 1555 1.44 LINK O4 NAG V 1 C1 NAG V 2 1555 1555 1.44 LINK O4 NAG W 1 C1 NAG W 2 1555 1555 1.44 LINK O4 NAG X 1 C1 NAG X 2 1555 1555 1.44 LINK O4 NAG X 2 C1 BMA X 3 1555 1555 1.45 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 1.000000 0.000000 0.000000 0.00000 SCALE2 0.000000 1.000000 0.000000 0.00000 SCALE3 0.000000 0.000000 1.000000 0.00000